PGLRB_ASPFA
ID PGLRB_ASPFA Reviewed; 367 AA.
AC P41750; A0A0D9MMX0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Endopolygalacturonase B;
DE EC=3.2.1.15;
DE AltName: Full=P1/P3;
DE AltName: Full=PGL;
DE AltName: Full=Pectinase B;
DE AltName: Full=Polygalacturonase B;
DE Flags: Precursor;
GN Name=pgaB; Synonyms=pecB; ORFNames=P034_00381312;
OS Aspergillus flavus (strain ATCC MYA-384 / AF70).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392242;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=ATCC MYA-384 / AF70;
RX PubMed=7574642; DOI=10.1128/aem.61.9.3316-3322.1995;
RA Whitehead M.P., Shieh M.T., Cleveland T.E., Cary J.W., Dean R.A.;
RT "Isolation and characterization of polygalacturonase genes (pecA and pecB)
RT from Aspergillus flavus.";
RL Appl. Environ. Microbiol. 61:3316-3322(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-384 / AF70;
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus flavus AF70.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC the smooth region of the plant cell wall. {ECO:0000269|PubMed:7574642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Expressed in presence of pectin when glucose is absent.
CC {ECO:0000269|PubMed:7574642}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U05020; AAA85280.1; -; Unassigned_DNA.
DR EMBL; JZDT01000916; KJJ28976.1; -; Genomic_DNA.
DR AlphaFoldDB; P41750; -.
DR SMR; P41750; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; EED53441; EED53441; AFLA_108160.
DR Proteomes; UP000032444; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..30
FT /evidence="ECO:0000255"
FT /id="PRO_0000024766"
FT CHAIN 31..367
FT /note="Endopolygalacturonase B"
FT /id="PRO_0000024767"
FT REPEAT 161..191
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 192..213
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 214..234
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 243..264
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 272..294
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 206
FT /note="Proton donor"
FT ACT_SITE 228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 34..49
FT /evidence="ECO:0000250"
FT DISULFID 208..224
FT /evidence="ECO:0000250"
FT DISULFID 334..339
FT /evidence="ECO:0000250"
FT DISULFID 358..367
FT /evidence="ECO:0000250"
FT CONFLICT 7..15
FT /note="GLAALGSLA -> VLAPLALSS (in Ref. 1; AAA85280)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="Missing (in Ref. 1; AAA85280)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="G -> V (in Ref. 1; AAA85280)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="T -> P (in Ref. 1; AAA85280)"
FT /evidence="ECO:0000305"
FT CONFLICT 135..145
FT /note="YAHKLQSSTIK -> QYPQLESPTIT (in Ref. 1; AAA85280)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="S -> T (in Ref. 1; AAA85280)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="Q -> L (in Ref. 1; AAA85280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 37798 MW; 98951FF0FC242576 CRC64;
MHFQLLGLAA LGSLAAAAPA PSRTSELVER GSSCTFTSAA QASASAKSCS NIVLKNIAVP
AGETLDLSKA KDGATITFEG TTTFGYKEWK GPLIRFGGNK ITVTQAAGAV IDGQGSRWWD
GKGTNGGKTK PKFIYAHKLQ SSTIKGLHVK NSPVQVFSVQ GNDVHLTDIT IDNSDGDNNG
GHNTDAFDVS ESNGVYITGA NVKNQDDCLA INSGENIEFT GATCSGGHGI SIGSIGNRDS
NTVKNVKVAD STVVDSDNGI RIKTISGATG SVSGVTYENI TLKNIKKNGI VIEQDYKNGG
PTGKPTTGVP ITDLTVNGVT GSVASKATPV YILCGKGSCS DWTWKGVSIS GGKKSDKCQN
IPSGASC
